William J. Booth
University of Sydney
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Publication
Featured researches published by William J. Booth.
Thrombosis Research | 1991
A. V. Mazurov; Dimitry V. Vinogradov; Tatjana N. Vlasik; V. S. Repin; William J. Booth; Michael C. Berndt
Platelet glycoprotein Ib (GPIb) acts as a high-affinity thrombin binding site and as a receptor for von Willebrand Factor (vWF). A new anti-GPIb monoclonal antibody (mAB) VM16d was produced that specifically inhibited platelet-thrombin but not platelet-vWF interaction. The epitope for VM16d was located within the 45 kDa N-terminal region of the alpha-chain of GPIb. VM16d inhibited platelet aggregation induced by low dose thrombin (0.05 U/ml) but did not affect platelet aggregation induced by ristocetin, bovine vWF, ADP or collagen. The same inhibitory effects on thrombin-induced platelet aggregation were observed with the whole IgG molecule of VM16d and its F(ab)2 and F(ab) fragments. VM16d also inhibited 14C-serotonin secretion induced by low dose thrombin and binding of 125I-thrombin but not ristocetin-dependent binding of 125I-vWF to platelets. These data indicate that the high-affinity thrombin binding site is located on the N-terminal 45 kDa domain of GPIb and that it is topographically separated from the vWF binding site.
Biochemical and Biophysical Research Communications | 1984
William J. Booth; Fiona H. Furby; Michael C. Berndt; P.A. Castaldi
Highly-purified plasma and platelet Factor VIII/von Willebrand Factor had potent lectin activity when measured in a haemagglutination assay. This lectin activity was inhibited by monoclonal and heterologous antibodies to Factor VIII/von Willebrand Factor as well as by hexosamines, mannose and net-positively charged amino acids.
Thrombosis Research | 1982
P.A. Castaldi; Michael C. Berndt; William J. Booth; C. Gregory; H. Bull; M. Greaves
Bleeding and abnormal platelet aggregation occur in patients with myeloproliferative disorders. In this study, twenty patients were examined, some sequentially, and a proportion found to have defective aggregation toward adrenaline, adenosine diphosphate (ADP), and collagen. In these seven patients, the abnormality in platelet response with defective collagen-induced [14C]serotonin release correlated with poor collagen-stimulated thromboxane B2 (TXB2) production. In contrast, five of these patients showed a normal threshold aggregation response to arachidonic acid. The combined results suggest that in these patients, there is a defect between receptor-stimulus coupling and the mobilization of arachidonic acid from membrane phospholipid.
Thrombosis Research | 1985
William J. Booth; P.A. Castaldi; Michael C. Berndt
Thrombospondin released from human blood platelets by thrombin activation formed high molecular weight aggregates which co-eluted with haemagglutinin activity on Sepharose 4B gel filtration. Thrombospondin aggregation was mediated by intermolecular disulphide bridges. The aggregates consisted of a series of oligomers ranging from a dimer to polymeric forms with Mr congruent to 40 X 10(6). Native monomeric thrombospondin obtained by a modified procedure was deficient in haemagglutination activity but inhibited haemagglutination induced by aggregated thrombospondin.
Biochemistry | 1989
Robert K. Andrews; William J. Booth; Jeffrey J. Gorman; Peter A. Castaldi; Michael C. Berndt
Biochemistry | 1988
Michael C. Berndt; Xiaoping Du; William J. Booth
Biochemistry | 1989
Robert K. Andrews; Jeffrey J. Gorman; William J. Booth; Gary L. Corino; Peter A. Castaldi; Michael C. Berndt
Biochemistry | 1992
Michael C. Berndt; Christopher Ward; William J. Booth; Peter A. Castaldi; A. V. Mazurov; Robert K. Andrews
Seminars in Thrombosis and Hemostasis | 1987
William J. Booth; Michael C. Berndt
Nouvelle revue française d'hématologie | 1992
Du X; William J. Booth; P.A. Castaldi; Michael C. Berndt
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Commonwealth Scientific and Industrial Research Organisation
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